Gimmel'reikh N G
Biokhimiia. 1975 Sep-Oct;40(5):1047-52.
Bivalent cations (Mn and Co) are found to activate ATPase activity of sarcolemma in the same degree, as Mg and Ca. The increase of the activity of Ca2+-dependent ATPase under the certain conditions of treatment of sarcolemma with KCl-Triton X-100 solution is not accompanied by the increase of ATPase activity in the presence of Mn and Co ions. ATPase activities in the presence of these ions correlate with the activity of Mg2+-dependent ATPase. Bivalent cations Mg, Mn and Co are competitive inhibitors for Ca2+-dependent ATPase. The apparent inhibition constants are determined to be 3,5-10(-5) M for Mg, 0,7-10(-3) M for Co and 1,5-10(-3) M for Mn. It is supposed that Ca2+-dependent ATPase has similar selectivity to bivalent cations as calcium influx that follows depolartization of plasma membrane.
已发现二价阳离子（锰和钴）与镁和钙一样，能同等程度地激活肌膜的ATP酶活性。在用氯化钾 - 曲拉通X - 100溶液处理肌膜的特定条件下，钙依赖性ATP酶活性的增加并未伴随着在锰和钴离子存在时ATP酶活性的增加。在这些离子存在下的ATP酶活性与镁依赖性ATP酶的活性相关。二价阳离子镁、锰和钴是钙依赖性ATP酶的竞争性抑制剂。确定镁的表观抑制常数为3.5×10⁻⁵ M，钴为0.7×10⁻³ M，锰为1.5×10⁻³ M。据推测，钙依赖性ATP酶对二价阳离子的选择性与质膜去极化后钙内流的选择性相似。
